Combining with a purine nucleotide and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.

Combining with an extracellular signal and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.

In order to isolate new subtypes of P2Y purinoceptors, a human placenta cDNA library was screened at middle stringency with a P2Y4 probe. The purification and the sequencing of several clones led us to identify a 984 base pair open reading frame encoding a new human P2Y receptor. It appeared later that this sequence corresponds to the human ortholog (88% amino acid identity) of the rat receptor recently cloned by Chang et al (J. Biol. Chem. 270, 26152-26158, 1995) and called P2Y6. Northern blot analysis detected human P2Y6 receptor messenger RNA in human spleen, placenta, thymus, intestine, and blood leukocytes. In 1321N1 cells stably expressing the human P2Y6 receptor, the formation of IP3 was stimulated by nucleotides with the following order of potency: UDP > 5-bromo-UPT > UTP > ADP > 2-methylthio-ATP >> ATP. The P2Y6 receptor, together with the previously cloned P2Y4 subtype (Communi et al., J. Biol. Chem., 270, 30849-30852, 1995), belongs thus to a subfamily of pyrimidinoceptors inside the P2Y family.

Just as reference genome sequences revolutionized human genetics, reference maps of interactome networks will be critical to fully understand genotype-phenotype relationships. Here, we describe a systematic map of ?14,000 high-quality human binary protein-protein interactions. At equal quality, this map is ?30% larger than what is available from small-scale studies published in the literature in the last few decades. While currently available information is highly biased and only covers a relatively small portion of the proteome, our systematic map appears strikingly more homogeneous, revealing a "broader" human interactome network than currently appreciated. The map also uncovers significant interconnectivity between known and candidate cancer gene products, providing unbiased evidence for an expanded functional cancer landscape, while demonstrating how high-quality interactome models will help "connect the dots" of the genomic revolution.

The series of molecular signals generated as a consequence of a receptor binding to an extracellular purine nucleotide and transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity.

The series of molecular signals generated as a consequence of a G-protein coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).

In order to isolate new subtypes of P2Y purinoceptors, a human placenta cDNA library was screened at middle stringency with a P2Y4 probe. The purification and the sequencing of several clones led us to identify a 984 base pair open reading frame encoding a new human P2Y receptor. It appeared later that this sequence corresponds to the human ortholog (88% amino acid identity) of the rat receptor recently cloned by Chang et al (J. Biol. Chem. 270, 26152-26158, 1995) and called P2Y6. Northern blot analysis detected human P2Y6 receptor messenger RNA in human spleen, placenta, thymus, intestine, and blood leukocytes. In 1321N1 cells stably expressing the human P2Y6 receptor, the formation of IP3 was stimulated by nucleotides with the following order of potency: UDP > 5-bromo-UPT > UTP > ADP > 2-methylthio-ATP >> ATP. The P2Y6 receptor, together with the previously cloned P2Y4 subtype (Communi et al., J. Biol. Chem., 270, 30849-30852, 1995), belongs thus to a subfamily of pyrimidinoceptors inside the P2Y family.

Keywords

Receptors which transduce extracellular signals across the cell membrane. At the external side they receive a ligand (a photon in case of opsins), and at the cytosolic side they activate a guanine nucleotide-binding (G) protein. These receptors are hydrophobic proteins that cross the membrane seven times.

Protein which is part of a reference proteome. Reference proteomes are a subset of proteomes that have been selected either manually or algorithmically according to a number of criteria to provide a broad coverage of the tree of life and a representative cross-section of the taxonomic diversity found within UniProtKB, as well as the proteomes of well-studied model organisms and other species of interest for biomedical research.